Počet záznamů: 1

Isolation of recombinant cysteine dioxygenase protein from Trichophyton mentagrophytes

SYSNO ASEP	0368595
Druh ASEP	J - Článek v odborném periodiku
Zařazení RIV	J - Článek v odborném periodiku
Poddruh J	Článek ve WOS
Název	Isolation of recombinant cysteine dioxygenase protein from Trichophyton mentagrophytes
Tvůrce(i)	Kašperová, A. (CZ) Kunert, J. (CZ) Horynová, M. (CZ) Weigl, E. (CZ) Sebela, M. (CZ) Lenobel, René (UEB-Q)_ORCID Raška, M. (CZ)
Celkový počet autorů	7
Zdroj.dok.	Mycoses. - : Wiley - ISSN 0933-7407 Roč. 54, č. 5 (2011), E456-E462
Poč.str.	7 s.
Jazyk dok.	eng - angličtina
Země vyd.	DE - Německo
Klíč. slova	Cysteine dioxygenase ; dermatophytes ; recombinant protein ; keratinolytic fungi ; cDNA
Vědní obor RIV	CE - Biochemie
CEP	GA301/08/1649 GA ČR - Grantová agentura ČR
CEZ	AV0Z50380511 - UEB-Q (2005-2011)
UT WOS	000294878900118
DOI	10.1111/j.1439-0507.2010.01948.x
Anotace	Cysteine dioxygenase (CDO, EC 1.13.11.20) catalyses the oxygenation of cysteine to cysteine sulphinic acid leading to the production of sulphite, sulphate and taurine as the final metabolites of cysteine catabolism. Keratinolytic fungi secrete sulphite and sulphate to reduce disulphide bridges in host tissue keratin proteins as the first step of keratinolysis. In the present study, we describe the identification of cDNA, as well as expression and characterisation of recombinant CDO protein from Trichophyton mentagrophytes. The cDNA was amplified using primers designed on the basis of high conservancy CDO regions identified in other fungi. PCR product was cloned and sequenced. Recombinant CDO was expressed in Escherichia colt, and affinity purified and identified by matrix-assisted laser desorption/ionization - time-of-flight mass spectrometry (MALDI-TOF MS). Enzyme activity was assayed by monitoring the production of cysteine sulphinate using mass spectrometry.
Pracoviště	Ústav experimentální botaniky
Kontakt	David Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469
Rok sběru	2012

Počet záznamů: 1